BRENDA - Enzyme Database
show all sequences of 2.5.1.104

N1-aminopropylagmatine, a new polyamine produced as a key intermediate in polyamine biosynthesis of an extreme thermophile, Thermus thermophilus

Ohnuma, M.; Terui, Y.; Tamakoshi, M.; Mitome, H.; Niitsu, M.; Samejima, K.; Kawashima, E.; Oshima, T.; J. Biol. Chem. 280, 30073-30082 (2005)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Thermus thermophilus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.77
-
agmatine
pH 9.0, 37°C
Thermus thermophilus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32500
-
x * 32500, SDS-PAGE
Thermus thermophilus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl 3-(methylthio)propylamine + agmatine
Thermus thermophilus
the enzyme is involved in polyamine biosynthesis
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermus thermophilus
Q5SK28
-
-
Purification (Commentary)
Commentary
Organism
-
Thermus thermophilus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.4
-
pH 8.5, 60°C
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl 3-(methylthio)propylamine + agmatine
-
719832
Thermus thermophilus
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + agmatine
the enzyme is involved in polyamine biosynthesis
719832
Thermus thermophilus
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 32500, SDS-PAGE
Thermus thermophilus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Thermus thermophilus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.37
-
agmatine
pH 9.0, 37°C
Thermus thermophilus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Thermus thermophilus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Thermus thermophilus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.77
-
agmatine
pH 9.0, 37°C
Thermus thermophilus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32500
-
x * 32500, SDS-PAGE
Thermus thermophilus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl 3-(methylthio)propylamine + agmatine
Thermus thermophilus
the enzyme is involved in polyamine biosynthesis
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermus thermophilus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.4
-
pH 8.5, 60°C
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl 3-(methylthio)propylamine + agmatine
-
719832
Thermus thermophilus
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
-
?
S-adenosyl 3-(methylthio)propylamine + agmatine
the enzyme is involved in polyamine biosynthesis
719832
Thermus thermophilus
5'-S-methyl-5'-thioadenosine + N1-aminopropylagmatine
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 32500, SDS-PAGE
Thermus thermophilus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Thermus thermophilus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.37
-
agmatine
pH 9.0, 37°C
Thermus thermophilus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
-
assay at
Thermus thermophilus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
480
-
agmatine
pH 9.0, 37°C
Thermus thermophilus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
480
-
agmatine
pH 9.0, 37°C
Thermus thermophilus
Other publictions for EC 2.5.1.104
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
720250
Ohnuma
Crystal structures and enzymat ...
Thermus thermophilus
J. Mol. Biol.
408
971-986
2011
-
-
1
1
-
-
-
5
-
-
2
-
-
3
-
-
1
-
-
-
-
-
7
1
1
-
-
5
3
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
5
-
-
2
-
-
-
-
1
-
-
-
-
7
1
1
-
-
5
3
-
1
-
-
-
-
-
5
5
719718
Morimoto
Dual biosynthesis pathway for ...
Thermococcus kodakarensis
J. Bacteriol.
192
4991-5001
2010
-
-
1
-
-
-
-
3
-
-
-
1
-
1
-
-
1
-
-
-
-
-
4
-
1
-
-
3
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
1
-
-
-
-
4
-
1
-
-
3
1
-
-
-
-
-
-
-
3
3
719710
Cacciapuoti
The first agmatine/cadaverine ...
Pyrococcus furiosus
J. Bacteriol.
189
6057-6067
2007
-
-
1
1
-
-
-
4
-
-
3
2
-
5
-
-
1
-
-
-
-
-
7
1
2
1
2
4
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
4
-
-
3
2
-
-
-
1
-
-
-
-
7
1
2
1
2
4
1
-
-
-
-
-
-
-
4
4
719832
Ohnuma
N1-aminopropylagmatine, a new ...
Thermus thermophilus
J. Biol. Chem.
280
30073-30082
2005
-
-
1
-
-
-
-
1
-
-
1
1
-
1
-
-
1
-
-
-
1
-
2
1
1
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
1
1
-
-
-
1
-
-
1
-
2
1
1
-
-
1
1
-
-
-
-
-
-
-
1
1